Librizzi Fabio, Rischel Christian
Dipartimento di Scienze Fisiche e Astronomiche, Via Archirafi 36, 90123 Palermo, Italy.
Protein Sci. 2005 Dec;14(12):3129-34. doi: 10.1110/ps.051692305.
When subjected to acidic conditions and high temperature, insulin is known to produce fibrils that display the common properties of disease amyloids. Thus, clarifying the mechanisms of insulin fibrillation can help the general understanding of amyloidal aggregation. Insulin fibrillation exhibits a very sharp time dependence, with a pronounced lag phase and subsequent explosive growth of amyloidal aggregates. Here we show that the initial stages of this process can be well described by exponential growth of the fibrillated proteins. This indicates that the process is mainly controlled by a secondary nucleation pathway.
已知在酸性条件和高温下,胰岛素会形成具有疾病淀粉样蛋白共同特性的纤维。因此,阐明胰岛素纤维化的机制有助于全面了解淀粉样聚集。胰岛素纤维化表现出非常明显的时间依赖性,具有明显的延迟期和随后淀粉样聚集体的爆发性增长。在这里,我们表明该过程的初始阶段可以通过纤维化蛋白的指数增长很好地描述。这表明该过程主要由二次成核途径控制。